Eksperimental'naia i klinicheskaia farmakologiia 2013-01-01

[Studying kinetics of oxime-induced reactivation of malathion-inhibited cholinesterase].

M A Iudin, D V Lantukhov, N G Vengerovich

Index: Eksp. Klin. Farmakol. 76(1) , 21-4, (2013)

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Abstract

The kinetics of oxime-induced reactivation of malathion-inhibited cholinesterase has been experimentally studied in vitro. It is shown that oximes do not restore the activity of inhibited butyrylcholinesterase. Acetylcholinesterase reactivation peak (5-mins long) was found to take place upon introduction of dipyroxime (32.5%), pralidoxime (18%), carboxyme (16%) at a concentration of 2.5 x 10(-4) mol/l or toxogonine (26%) at a concentration of 5 x 10(-4) mol/l. Toxogonine demonstrated the maximum affinity to phosphorylated enzyme, while dipyroxime is characterized by a high reactivity with respect to oxime. Significant reactivating ability of these preparations (kR -2300 mol(-1) min(-1) makes them promising solution for the treatment of malathion intoxication.